Nucleic Acids Research, Vol 26, Issue 3 803-809, Copyright © 1998 by Oxford University Press
B Schwer, P Linder and S Shuman
The homologous Saccharomyces cerevisiae genes CES1 and CES4 act as high
copy suppressors of temperature-sensitive mutations of Ceg1p, the yeast
mRNA capping enzyme. Neither CES1 nor CES4 is essential for cell growth. We
find that a double deletion mutant (Delta ces1 Delta ces4 ) grows at 25-37
degrees C, but not at 16 degrees C. Delta ces1 Delta ces4 cells display
gross defects in cell shape and budding even at permissive temperatures.
Functional analysis of CES1 deletion mutants defines a 145 amino acid
C-terminal segment of the 915 amino acid Ces1 protein that is necessary and
sufficient to complement the Delta ces1 Delta ces 4 cold-sensitive
phenotype, to restore normal morphology and to suppress the
temparature-sensitive mutant ceg1-25 . A 147 amino acid C-terminal segment
of the 942 amino acid Ces4 protein is sufficient to carry out these same
functions. Within this carboxyl domain Ces1p and Ces4p are 80% identical to
one another. We report isolation of CES1 in a separate screen for high copy
suppression of a temperature-sensitive mutation (A79V) of the yeast
translation initiation factor Tif1p (eIF- 4A). Deletion of the N-terminal
249 amino acids of Ces1p abolished tif1- A79V suppressor function. CES4 on
a multicopy plasmid was unable to suppress tif1-A79V . We surmise that
whereas the carboxyl domains of Ces1p and Ces4p are functionally redundant
in controlling cell morphology and in suppressing ceg1-25 , full-length
Ces1p and Ces4p evince distinct genetic interactions that are likely
mediated by their N-terminal segments.
ARTICLES
Effects of deletion mutations in the yeast Ces1 protein on cell growth and morphology and on high copy suppression of mutations in mRNA capping enzyme and translation initiation factor 4A
Department of Microbiology, Cornell University Medical College, New York, NY 10021, USA.
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